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Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase); Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC)]

 PUR6_HUMAN              Reviewed;         425 AA.
P22234; E9PDH9; Q68CQ5;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 197.
RecName: Full=Multifunctional protein ADE2;
Includes:
RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
EC=6.3.2.6;
AltName: Full=SAICAR synthetase;
Includes:
RecName: Full=Phosphoribosylaminoimidazole carboxylase;
EC=4.1.1.21;
AltName: Full=AIR carboxylase;
Short=AIRC;
Name=PAICS; Synonyms=ADE2, AIRC, PAIS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2253271; DOI=10.1007/BF00318209;
Minet M., Lacroute F.;
"Cloning and sequencing of a human cDNA coding for a multifunctional
polypeptide of the purine pathway by complementation of the ade2-101
mutant in Saccharomyces cerevisiae.";
Curr. Genet. 18:287-291(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
Submitted (JUL-2004) to UniProtKB.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-238, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-107, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-107; THR-238 AND
SER-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ACTIVE SITE, AND
MUTAGENESIS OF HIS-303; SER-332 AND GLY-334.
PubMed=17224163; DOI=10.1016/j.jmb.2006.12.027;
Li S.-X., Tong Y.-P., Xie X.-C., Wang Q.-H., Zhou H.-N., Han Y.,
Zhang Z.-Y., Gao W., Li S.-G., Zhang X.C., Bi R.-C.;
"Octameric structure of the human bifunctional enzyme PAICS in purine
biosynthesis.";
J. Mol. Biol. 366:1603-1614(2007).
-!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D-
ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate +
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
carboxamido)succinate.
-!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2).
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-
amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step
1/1.
-!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:17224163}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-712261, EBI-712261;
P51116:FXR2; NbExp=3; IntAct=EBI-712261, EBI-740459;
Q969R5:L3MBTL2; NbExp=6; IntAct=EBI-712261, EBI-739909;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-712261, EBI-739832;
Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-712261, EBI-740486;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P22234-1; Sequence=Displayed;
Name=2;
IsoId=P22234-2; Sequence=VSP_041265;
-!- SIMILARITY: In the N-terminal section; belongs to the SAICAR
synthetase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the AIR
carboxylase family. Class II subfamily. {ECO:0000305}.
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EMBL; X53793; CAA37801.1; -; mRNA.
EMBL; BT006988; AAP35634.1; -; mRNA.
EMBL; CR749824; CAH18683.1; -; mRNA.
EMBL; AC068620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010273; AAH10273.1; -; mRNA.
EMBL; BC019255; AAH19255.1; -; mRNA.
CCDS; CCDS47060.1; -. [P22234-2]
CCDS; CCDS47061.1; -. [P22234-1]
PIR; S14147; S14147.
RefSeq; NP_001072992.1; NM_001079524.1. [P22234-1]
RefSeq; NP_001072993.1; NM_001079525.1. [P22234-2]
RefSeq; NP_006443.1; NM_006452.3. [P22234-1]
UniGene; Hs.518774; -.
UniGene; Hs.709570; -.
PDB; 2H31; X-ray; 2.80 A; A=1-425.
PDBsum; 2H31; -.
ProteinModelPortal; P22234; -.
SMR; P22234; -.
BioGrid; 115852; 94.
IntAct; P22234; 37.
MINT; P22234; -.
STRING; 9606.ENSP00000382595; -.
ChEMBL; CHEMBL5922; -.
DrugBank; DB00128; L-Aspartic Acid.
iPTMnet; P22234; -.
PhosphoSitePlus; P22234; -.
SwissPalm; P22234; -.
BioMuta; PAICS; -.
DMDM; 131628; -.
EPD; P22234; -.
MaxQB; P22234; -.
PaxDb; P22234; -.
PeptideAtlas; P22234; -.
PRIDE; P22234; -.
ProteomicsDB; 53968; -.
ProteomicsDB; 53969; -. [P22234-2]
DNASU; 10606; -.
Ensembl; ENST00000264221; ENSP00000264221; ENSG00000128050. [P22234-1]
Ensembl; ENST00000399688; ENSP00000382595; ENSG00000128050. [P22234-2]
Ensembl; ENST00000512576; ENSP00000421096; ENSG00000128050. [P22234-1]
GeneID; 10606; -.
KEGG; hsa:10606; -.
UCSC; uc003hbs.1; human. [P22234-1]
CTD; 10606; -.
DisGeNET; 10606; -.
EuPathDB; HostDB:ENSG00000128050.8; -.
GeneCards; PAICS; -.
HGNC; HGNC:8587; PAICS.
HPA; HPA035895; -.
HPA; HPA041538; -.
MIM; 172439; gene.
neXtProt; NX_P22234; -.
OpenTargets; ENSG00000128050; -.
PharmGKB; PA32914; -.
eggNOG; KOG2835; Eukaryota.
eggNOG; COG0041; LUCA.
eggNOG; COG0152; LUCA.
GeneTree; ENSGT00390000010172; -.
HOGENOM; HOG000082628; -.
HOVERGEN; HBG008335; -.
InParanoid; P22234; -.
KO; K01587; -.
OMA; WSDEQII; -.
OrthoDB; EOG091G08DN; -.
PhylomeDB; P22234; -.
TreeFam; TF106384; -.
BioCyc; MetaCyc:HS05155-MONOMER; -.
Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
UniPathway; UPA00074; UER00130.
UniPathway; UPA00074; UER00131.
ChiTaRS; PAICS; human.
EvolutionaryTrace; P22234; -.
GenomeRNAi; 10606; -.
PRO; PR:P22234; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000128050; Expressed in 226 organ(s), highest expression level in embryo.
CleanEx; HS_PAICS; -.
ExpressionAtlas; P22234; baseline and differential.
Genevisible; P22234; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; TAS:Reactome.
GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; TAS:Reactome.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009113; P:purine nucleobase biosynthetic process; TAS:ProtInc.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
Gene3D; 3.40.50.7700; -; 1.
HAMAP; MF_02045; PurE_classII; 1.
HAMAP; MF_00137; SAICAR_synth; 1.
InterPro; IPR033626; PurE_classII.
InterPro; IPR000031; PurE_dom.
InterPro; IPR035893; PurE_sf.
InterPro; IPR028923; SAICAR_synt/ADE2_N.
InterPro; IPR018236; SAICAR_synthetase_CS.
Pfam; PF00731; AIRC; 1.
Pfam; PF01259; SAICAR_synt; 1.
SMART; SM01001; AIRC; 1.
SUPFAM; SSF52255; SSF52255; 1.
TIGRFAMs; TIGR01162; purE; 1.
PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Decarboxylase; Direct protein sequencing; Ligase;
Lyase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Polymorphism; Purine biosynthesis; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.6}.
CHAIN 2 425 Multifunctional protein ADE2.
/FTId=PRO_0000075030.
REGION 2 260 SAICAR synthetase.
REGION 261 266 Linker.
REGION 267 425 AIR carboxylase.
ACT_SITE 101 101 For SAICAR synthetase activity.
{ECO:0000269|PubMed:17224163}.
ACT_SITE 107 107 For SAICAR synthetase activity.
{ECO:0000269|PubMed:17224163}.
ACT_SITE 215 215 For SAICAR synthetase activity.
{ECO:0000269|PubMed:17224163}.
ACT_SITE 303 303 For AIR carboxylase activity.
{ECO:0000269|PubMed:17224163}.
ACT_SITE 332 332 For AIR carboxylase activity.
{ECO:0000269|PubMed:17224163}.
SITE 334 334 Essential for AIR carboxylase activity.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.6}.
MOD_RES 22 22 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9DCL9}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 36 36 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9DCL9}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 238 238 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 247 247 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 72 72 G -> VTSYKSNR (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_041265.
VARIANT 201 201 K -> N (in dbSNP:rs11549976).
/FTId=VAR_051884.
MUTAGEN 303 303 H->Y: Loss of AIR carboxylase activity.
{ECO:0000269|PubMed:17224163}.
MUTAGEN 332 332 S->A: Loss of AIR carboxylase activity.
{ECO:0000269|PubMed:17224163}.
MUTAGEN 334 334 G->A: Loss of AIR carboxylase activity.
{ECO:0000269|PubMed:17224163}.
MUTAGEN 400 400 S->A: No change of AIR carboxylase
activity.
CONFLICT 217 217 W -> R (in Ref. 3; CAH18683).
{ECO:0000305}.
CONFLICT 340 340 S -> T (in Ref. 3; CAH18683).
{ECO:0000305}.
STRAND 20 22 {ECO:0000244|PDB:2H31}.
STRAND 32 35 {ECO:0000244|PDB:2H31}.
HELIX 54 71 {ECO:0000244|PDB:2H31}.
STRAND 82 88 {ECO:0000244|PDB:2H31}.
STRAND 91 93 {ECO:0000244|PDB:2H31}.
STRAND 97 103 {ECO:0000244|PDB:2H31}.
HELIX 106 111 {ECO:0000244|PDB:2H31}.
STRAND 126 130 {ECO:0000244|PDB:2H31}.
HELIX 142 146 {ECO:0000244|PDB:2H31}.
TURN 147 149 {ECO:0000244|PDB:2H31}.
HELIX 159 180 {ECO:0000244|PDB:2H31}.
HELIX 181 183 {ECO:0000244|PDB:2H31}.
STRAND 186 192 {ECO:0000244|PDB:2H31}.
STRAND 194 197 {ECO:0000244|PDB:2H31}.
TURN 198 200 {ECO:0000244|PDB:2H31}.
STRAND 203 205 {ECO:0000244|PDB:2H31}.
STRAND 213 217 {ECO:0000244|PDB:2H31}.
STRAND 241 243 {ECO:0000244|PDB:2H31}.
HELIX 249 253 {ECO:0000244|PDB:2H31}.
HELIX 256 260 {ECO:0000244|PDB:2H31}.
STRAND 267 273 {ECO:0000244|PDB:2H31}.
HELIX 275 277 {ECO:0000244|PDB:2H31}.
HELIX 278 290 {ECO:0000244|PDB:2H31}.
STRAND 295 299 {ECO:0000244|PDB:2H31}.
TURN 302 304 {ECO:0000244|PDB:2H31}.
HELIX 306 317 {ECO:0000244|PDB:2H31}.
STRAND 323 328 {ECO:0000244|PDB:2H31}.
HELIX 335 342 {ECO:0000244|PDB:2H31}.
STRAND 347 349 {ECO:0000244|PDB:2H31}.
TURN 355 357 {ECO:0000244|PDB:2H31}.
HELIX 358 361 {ECO:0000244|PDB:2H31}.
HELIX 362 364 {ECO:0000244|PDB:2H31}.
HELIX 380 392 {ECO:0000244|PDB:2H31}.
HELIX 396 421 {ECO:0000244|PDB:2H31}.
SEQUENCE 425 AA; 47079 MW; E08CF19BC8898F29 CRC64;
MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI
TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVKEGYK
FYPPKVELFF KDDANNDPQW SEEQLIAAKF CFAGLLIGQT EVDIMSHATQ AIFEILEKSW
LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE
GLQMVKKNFE WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT
SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC PPLTPDWGVQ
DVWSSLRLPS GLGCSTVLSP EGSAQFAAQI FGLSNHLVWS KLRASILNTW ISLKQADKKI
RECNL


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